Histone acetyltransferase Hbo1: Catalytic activity, cellular abundance, and links to primary cancers

Masayoshi Iizuka, Yoshihisa Takahashi, Craig A. Mizzen, Richard G. Cook, Masatoshi Fujita, C. David Allis, Henry F. Frierson, Toshio Fukusato, M. Mitchell Smith

研究成果: Contribution to journalArticle査読

66 被引用数 (Scopus)

抄録

In addition to the well-characterized proteins that comprise the pre-replicative complex, recent studies suggest that chromatin structure plays an important role in DNA replication initiation. One of these chromatin factors is the histone acetyltransferase (HAT) Hbo1 which is unique among HAT enzymes in that it serves as a positive regulator of DNA replication. However, several of the basic properties of Hbo1 have not been previously examined, including its intrinsic catalytic activity, its molecular abundance in cells, and its pattern of expression in primary cancer cells. Here we show that recombinant Hbo1 can acetylate nucleosomal histone H4 in vitro, with a preference for lysines 5 and 12. Using semi-quantitative western blot analysis, we find that Hbo1 is approximately equimolar with the number of active replication origins in normal human fibroblasts but is an order of magnitude more abundant in both MCF7 and Saos-2 established cancer cell lines. Immunohistochemistry for Hbo1 in 11 primary human tumor types revealed strong Hbo1 protein expression in carcinomas of the testis, ovary, breast, stomach/esophagus, and bladder.

本文言語英語
ページ(範囲)108-114
ページ数7
ジャーナルGene
436
1-2
DOI
出版ステータス出版済み - 5 1 2009
外部発表はい

All Science Journal Classification (ASJC) codes

  • 遺伝学

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